ID Q8DQ00_STRR6 Unreviewed; 358 AA. AC Q8DQ00; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 19-FEB-2014, entry version 75. DE RecName: Full=Aspartate-semialdehyde dehydrogenase; DE Short=ASA dehydrogenase; DE Short=ASADH; DE EC=1.2.1.11; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase; GN Name=asd; OrderedLocusNames=spr0918; OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=171101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-255 / R6; RX PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001; RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., RA LeBlanc D.J., Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., RA McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., RA Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., RA Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., RA Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., RA Glass J.I.; RT "Genome of the bacterium Streptococcus pneumoniae strain R6."; RL J. Bacteriol. 183:5709-5717(2001). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RX PubMed=22039970; DOI=10.1111/j.1747-0285.2011.01267.x; RA Pavlovsky A.G., Liu X., Faehnle C.R., Potente N., Viola R.E.; RT "Structural characterization of inhibitors with selectivity against RT members of a homologous enzyme family."; RL Chem. Biol. Drug Des. 79:128-136(2012). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate (By similarity). CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE007317; AAK99722.1; -; Genomic_DNA. DR PIR; F97986; F97986. DR RefSeq; NP_358512.1; NC_003098.1. DR PDB; 3Q1L; X-ray; 2.30 A; A/B/C/D=1-358. DR PDBsum; 3Q1L; -. DR ProteinModelPortal; Q8DQ00; -. DR SMR; Q8DQ00; 2-358. DR STRING; 171101.spr0918; -. DR EnsemblBacteria; AAK99722; AAK99722; spr0918. DR GeneID; 933797; -. DR KEGG; spr:spr0918; -. DR PATRIC; 19701775; VBIStrPne107296_1005. DR eggNOG; COG0136; -. DR HOGENOM; HOG000013357; -. DR KO; K00133; -. DR OMA; FPIKKFV; -. DR OrthoDB; EOG6JB158; -. DR ProtClustDB; PRK14874; -. DR BioCyc; SPNE171101:GJC8-930-MONOMER; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR005986; Asp_semialdehyde_DH_beta. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR TIGRFAMs; TIGR01296; asd_B; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome; KW Threonine biosynthesis. FT NP_BIND 11 14 NADP (By similarity). FT NP_BIND 39 40 NADP (By similarity). FT NP_BIND 158 159 NADP (By similarity). FT ACT_SITE 128 128 Acyl-thioester intermediate (By FT similarity). FT ACT_SITE 252 252 Proton acceptor (By similarity). FT BINDING 99 99 Phosphate (By similarity). FT BINDING 155 155 Substrate (By similarity). FT BINDING 245 245 Substrate (By similarity). FT BINDING 325 325 NADP (By similarity). SQ SEQUENCE 358 AA; 38924 MW; 366715956847C96C CRC64; MGYTVAVVGA TGAVGAQMIK MLEESTLPID KIRYLASARS AGKSLKFKDQ DITIEETTET AFEGVDIALF SAGSSTSAKY APYAVKAGVV VVDNTSYFRQ NPDVPLVVPE VNAHALDAHN GIIACPNCST IQMMVALEPV RQKWGLDRII VSTYQAVSGA GMGAILETQR ELREVLNDGV KPCDLHAEIL PSGGDKKHYP IAFNALPQID VFTDNDYTYE EMKMTKETKK IMEDDSIAVS ATCVRIPVLS AHSESVYIET KEVAPIEEVK AAIAAFPGAV LEDDVAHQIY PQAINAVGSR DTFVGRIRKD LDAEKGIHMW VVSDNLLKGA AWNSVQIAET LHERGLVRPT AELKFELK //